@article {1333,
	title = {The bogorol family of antibiotics: Template-based structure elucidation and a new approach to positioning enantiomeric pairs of amino acids},
	journal = {Journal of Organic Chemistry},
	volume = {71},
	number = {16},
	year = {2006},
	note = {ISI Document Delivery No.: 067XTTimes Cited: 10Cited Reference Count: 29Barsby, Todd Warabi, Kaoru Sorensen, Dan Zimmerman, William T. Kelly, Michael T. Andersen, Raymond J.},
	month = {Aug},
	pages = {6031-6037},
	type = {Article},
	abstract = {The sequence positions of D and L Leu and Lys residues in bogorol A (1) have been defined by a simple and novel approach that utilizes small amounts of sample and focuses on detecting the order in which amino acids are liberated from the parent peptide during acid-catalyzed hydrolysis. This technique builds on a previously established relationship between the steric and electronic features of amino acids and their predilection for acidic liberation from polypeptides via dipeptides. The results, which complete the structure of bogorol A, have been confirmed by traditional degradation experiments. Utilizing the knowledge of the structure of bogorol A (1) as a template, we rapidly elucidated the structures of bogorols B-E (2-5) via analysis of ESI-MS and ESI-MS/ MS data and GC analysis of degradation products. The bogorol cationic peptide antibiotics contain a number of unusual structural features, which include the reduction of the C-terminal residue to valinol, an N-terminal residue of 2-hydroxy-3-methylpentanoic acid, the incorporation of four D amino acids, and the presence of a dehydroamino acid. Bogorols show selective and relatively potent activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus spp., as well as moderate activity against Escherichia coli.},
	keywords = {ANTIMICROBIAL PEPTIDE, BACILLUS, CONVERSION, CULTURE, resistance, SYSTEM, THREONINE, TROPICAL MARINE BACTERIUM},
	isbn = {0022-3263},
	url = {<Go to ISI>://000239336600025},
	author = {Barsby, T. and Warabi, K. and Sorensen, D. and Zimmerman, W. T. and Kelly, M. T. and Andersen, R. J.}
}
@article {3549,
	title = {PRODUCTION AND PROPERTIES OF A BIFUNCTIONAL FUSION PROTEIN THAT MEDIATES ATTACHMENT OF VERO CELLS TO CELLULOSIC MATRICES},
	journal = {Biotechnology and Bioengineering},
	volume = {47},
	number = {2},
	year = {1995},
	note = {ISI Document Delivery No.: RD894Times Cited: 7Cited Reference Count: 29},
	month = {Jul},
	pages = {147-154},
	type = {Article},
	abstract = {The sequence Arg-Gly-Asp (RGD) in extracellular matrix proteins such as fibronectin, collagen, and laminin mediates cell attachment by interacting with proteins of the integrin family of cell surface receptors. A gene fusion encoding the RGD-containing peptide, fused to the C-terminus of a cellulose-binding domain (CBD/RGD), was expressed in Escherichia coli. Cultures produced up to 50 mg of CBD/RGD per titer, most of which was extracellular. it was purified from the culture supernatant by affinity chromatography on cellulose. CBD/RGD promoted the attachment of green monkey Vero cells to polystyrene and cellulose acetate. Attachment was inhibited by smalt synthetic peptides containing the RGD sequence. CBD/RGD was as effective as collagen in promoting the attachment of Vero cells to Cellsnow(TM) microcarriers. (C) 1995 John Wiley and Sons, Inc.},
	keywords = {ADHESION, ARG-GLY-ASP, BINDING DOMAINS, BIOTECHNOLOGY, CELLULASES, CELLULOMONAS-FIMI, CELLULOSE, CULTURE, FIBRONECTIN, PROTEIN PRODUCTION, SEGMENT, SIGNAL, VITRONECTIN},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1995RD89400004},
	author = {Wierzba, A. and Reichl, U. and Turner, R. F. B. and Warren, R. A. J. and Kilburn, D. G.}
}
